Pectate lyase - Bacillus sp.

Preferred order of sections

Names and origin

Protein names	Submitted name: Pectate lyase EMBL BAA87892.1
Organism	Bacillus sp. EMBL BAA87892.1
Taxonomic identifier	1409 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1EE6 Metal-binding PDB 1EE6
Molecular function	Lyase EMBL BAA87892.1
Technical term	3D-structure PDB 1EE6
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pectate lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

107

1

Calcium PDB 1EE6

Metal binding

108

1

Calcium; via carbonyl oxygen PDB 1EE6

Metal binding

130

1

Calcium; via carbonyl oxygen PDB 1EE6

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RHW0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 99D04821B09DE523
Show »

FASTA

224

23,751

        10         20         30         40         50         60 
MKKLLGLILS AALTLSLYGL EPQVAEAAPT VVHETIRVPA GQTFDGKGQT YVANPNTLGD 

        70         80         90        100        110        120 
GSQAENQKPI FRLEAGASLK NVVIGAPAAD GVHCYGDCTI TNVIWEDVGE DALTLKSSGT 

       130        140        150        160        170        180 
VNISGGAAYK AYDKVFQINA AGTINIRNFR ADDIGKLVRQ NGGTTYKVVM NVENCNISRV 

       190        200        210        220 
KDAILRTDSS TSTGRIVNTR YSNVPTLFKG FKSGNTTASG NTQY

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References

[1]	"Deduced amino-acid sequence and possible catalytic residues of a novel pectate lyase from an alkaliphilic strain of Bacillus." Hatada Y., Saito K., Koike K., Yoshimatsu T., Ozawa T., Kobayashi T., Ito S. Eur. J. Biochem. 267:2268-2275(2000) [PubMed: 10759850] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: KSM-P15 EMBL BAA87892.1.
[2]	"The first structure of pectate lyase belonging to polysaccharide lyase family 3." Akita M., Suzuki A., Kobayashi T., Ito S., Yamane T. Acta Crystallogr. D Biol. Crystallogr. 57:1786-1792(2001) [PubMed: 11717490] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 28-224 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB011839 Genomic DNA. Translation: BAA87892.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EE6	X-ray	2.30	A	28-224	[»]

ProteinModelPortal

Q9RHW0.

SMR

Q9RHW0. Positions 28-224.

ModBase

Search...

Protein family/group databases

CAZy

PL3. Polysaccharide Lyase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

4.2.2.2. 1000.

Family and domain databases

InterPro

IPR004898. Pectate_lyase_cat.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]

Gene3D

G3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.

Pfam

PF03211. Pectate_lyase. 1 hit.
[Graphical view]

SUPFAM

SSF51126. Pectin_lyas_like. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q9RHW0_BACSP

Accession

Primary (citable) accession number: Q9RHW0

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	February 8, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)